FTSW_MYCTU
ID FTSW_MYCTU Reviewed; 524 AA.
AC P9WN97; L0T901; O06223; P63762;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000250|UniProtKB:P39604};
DE Short=PGT {ECO:0000250|UniProtKB:P39604};
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P39604};
DE AltName: Full=Cell division protein FtsW {ECO:0000250|UniProtKB:O07639};
DE AltName: Full=Cell wall polymerase {ECO:0000250|UniProtKB:P39604};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000250|UniProtKB:P39604};
DE Short=PG polymerase {ECO:0000250|UniProtKB:P39604};
GN Name=ftsW; OrderedLocusNames=Rv2154c; ORFNames=MTCY270.14;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INTERACTION WITH FTSZ, AND DOMAIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12101218; DOI=10.1074/jbc.m203847200;
RA Datta P., Dasgupta A., Bhakta S., Basu J.;
RT "Interaction between FtsZ and FtsW of Mycobacterium tuberculosis.";
RL J. Biol. Chem. 277:24983-24987(2002).
RN [3]
RP SUBUNIT, INTERACTION WITH PBPB, SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RX PubMed=17427288; DOI=10.1111/j.1365-2958.2006.05491.x;
RA Datta P., Dasgupta A., Singh A.K., Mukherjee P., Kundu M., Basu J.;
RT "Interaction between FtsW and penicillin-binding protein 3 (PBP3) directs
RT PBP3 to mid-cell, controls cell septation and mediates the formation of a
RT trimeric complex involving FtsZ, FtsW and PBP3 in mycobacteria.";
RL Mol. Microbiol. 62:1655-1673(2006).
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC {ECO:0000250|UniProtKB:P39604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000250|UniProtKB:P39604};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000250|UniProtKB:P39604}.
CC -!- SUBUNIT: Forms a complex with FtsZ and PbpB (PBP3, FtsI).
CC {ECO:0000269|PubMed:17427288}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17427288};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17427288}.
CC Note=Localizes to the division septum. {ECO:0000250}.
CC -!- DOMAIN: Interacts with FtsZ via its C-terminal region, and with PbpB
CC via two extracytoplasmic loops. {ECO:0000269|PubMed:12101218,
CC ECO:0000269|PubMed:17427288}.
CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44930.1; -; Genomic_DNA.
DR PIR; F70579; F70579.
DR RefSeq; NP_216670.1; NC_000962.3.
DR RefSeq; WP_003411165.1; NZ_NVQJ01000044.1.
DR AlphaFoldDB; P9WN97; -.
DR SMR; P9WN97; -.
DR STRING; 83332.Rv2154c; -.
DR PaxDb; P9WN97; -.
DR DNASU; 887916; -.
DR GeneID; 887916; -.
DR KEGG; mtu:Rv2154c; -.
DR TubercuList; Rv2154c; -.
DR eggNOG; COG0772; Bacteria.
DR OMA; KLWWSNL; -.
DR PhylomeDB; P9WN97; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR InterPro; IPR013437; FtsW.
DR InterPro; IPR001182; FtsW/RodA.
DR PANTHER; PTHR30474; PTHR30474; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR TIGRFAMs; TIGR02614; ftsW; 1.
DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..524
FT /note="Probable peptidoglycan glycosyltransferase FtsW"
FT /id="PRO_0000062725"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..151
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 56337 MW; C98052A346739C7C CRC64;
MLTRLLRRGT SDTDGSQTRG AEPVEGQRTG PEEASNPGSA RPRTRFGAWL GRPMTSFHLI
IAVAALLTTL GLIMVLSASA VRSYDDDGSA WVIFGKQVLW TLVGLIGGYV CLRMSVRFMR
RIAFSGFAIT IVMLVLVLVP GIGKEANGSR GWFVVAGFSM QPSELAKMAF AIWGAHLLAA
RRMERASLRE MLIPLVPAAV VALALIVAQP DLGQTVSMGI ILLGLLWYAG LPLRVFLSSL
AAVVVSAAIL AVSAGYRSDR VRSWLNPEND PQDSGYQARQ AKFALAQGGI FGDGLGQGVA
KWNYLPNAHN DFIFAIIGEE LGLVGALGLL GLFGLFAYTG MRIASRSADP FLRLLTATTT
LWVLGQAFIN IGYVIGLLPV TGLQLPLISA GGTSTAATLS LIGIIANAAR HEPEAVAALR
AGRDDKVNRL LRLPLPEPYL PPRLEAFRDR KRANPQPAQT QPARKTPRTA PGQPARQMGL
PPRPGSPRTA DPPVRRSVHH GAGQRYAGQR RTRRVRALEG QRYG
